Structural Characterization of MacroH2A Containing Chromatin

Biochemistry

Volumn 43, Issue 5, 2004, Pages 1352-1359

  Abbott, D Wade ^a   Laszczak, Mario ^a   Lewis, John D ^a   Su, Harvey ^a,b   Moore, Susan C ^a,c   Hills, Melissa ^a   Dimitrov, Stefan ^d   Ausió, Juan ^a  

^a UNIVERSITY OF VICTORIA   (Canada)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^c VANCOUVER GENERAL HOSPITAL   (Canada)

^d INSTITUT ALBERT BONNIOT   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; PROTEINS; TISSUE;

HISTONES;

BIOCHEMISTRY;

HISTONE; HISTONE H2A; ISOPROTEIN; MACROH2A PROTEIN; UNCLASSIFIED DRUG;

ACETYLATION; ALPHA HELIX; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CHROMATIN; HUMAN; HUMAN CELL; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN VARIANT; STRUCTURE ANALYSIS; TISSUE DISTRIBUTION;

ACETYLATION; ANIMALS; CHICKENS; CHROMATIN; ERYTHROCYTES; HELA CELLS; HISTONES; HUMANS; ICTALURIDAE; LIVER; MALE; NUCLEOSOMES; ORGAN SPECIFICITY; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RANA CATESBEIANA; TESTIS; ULTRACENTRIFUGATION;

ANIMALIA; VERTEBRATA;

EID: 0842347934     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035859i     Document Type: Article

References (62)

1. Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution, Nature 389, 251-260.
2. Knezetic, J. A., and Luse, D. S. (1986) The presence of nucleosomes on a DNA template prevents initiation by RNA polymerase II in vitro, Cell 45, 95-104.
3. Matsui, T. (1987) Transcription of adenovirus 2 major late and peptide IX genes under conditions of in vitro nucleosome assembly, Mol. Cell. Biol. 7, 1401-1408.
4. Wilkins, R. J., and Hart, R. W. (1974) Preferential DNA repair in human cells, Nature 247, 35-36.
5. Wang, Z. G., Wu, X. H., and Friedberg, E. C. (1991) Nucleotide excision repair of DNA by human cell extracts is suppressed in reconstituted nucleosomes, J. Biol. Chem. 266, 22472-22478.
6. Sugasawa, K., Masutani, C., and Hanaoka, F. (1993) Cell-free repair of UV-damaged simian virus 40 chromosomes in human cell extracts. I. Development of a cell-free system detecting excision repair of UV-irradiated SV40 chromosomes, J. Biol. Chem. 268, 9098-9104.
7. Strahl, B. D., and Allis, C. D. (2000) The language of covalent histone modifications, Nature 403, 41-45.
8. Turner, B. M. (2000) Histone acetylation and an epigenetic code, Bioessays 22, 836-845.
9. Ausió, J., Abbott, D. W., Wang, X., and Moore, S. C. (2001) Histone variants and histone modifications: a structural perspective, Biochem. Cell Biol. 79, 693-708.
10. Ausió, J., and Abbott, D. W. (2002) The many tales of a tail: carboxyl-terminal tail heterogeneity specializes histone H2A variants for defined chromatin function. Biochemistry 41, 5945-5949.
11. Wolffe, A. P., and Dimitrov, S. (1993) Histone-modulated gene activity: developmental implications, Crit. Rev. Eukaryot. Gene Expr. 3. 167-191.
12. Alvelo-Ceron, D., Niu, L., and Collart, D. G. (2000) Growth regulation of human variant histone genes and acetylation of the encoded proteins, Mol. Biol. Rep. 27, 61-71.
13. Pehrson, J. R., and Fried, V. A. (1992) MacroH2A, a core histone containing a large nonhistone region, Science 257, 1398-1400.
14. Chadwick, B. P., and Willard, H. F. (2002) Cell cycle-dependent localization of macroH2A in chromatin of the inactive X chromosome, J. Cell Biol. 157, 1113-1123.
15. Changolkar, L. N., and Pehrson, J. R. (2002) Reconstitution of nucleosomes with histone macroH2A1.2, Biochemistry 41, 179-184.
16. Angelov, D., Molla, A., Perche, P. Y., Hans, F., Cote, J., Khochbin, S., Bouvet, P., and Dimitrov, S. (2003) The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling, Mol. Cell 11, 1033-1041.
17. Pehrson, J. R., Costanzi, C., and Dharia, C. (1997) Developmental and tissue expression patterns of histone macroH2A1 subtypes, J. Cell. Biochem. 65, 107-113.
18. Costanzi, C., and Pehrson, J. R. (1998) Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals, Nature 393, 599-601.
19. Costanzi, C., Stein, P., Worrad, D. M., Schultz, R. M., and Pehrson, J. R. (2000) Histone macroH2A1 is concentrated in the inactive X chromosome of female preimplantation mouse embryos, Development 127, 2283-2289.
20. Chadwick, B. P., and Willard, H. F. (2001) A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome, J. Cell Biol. 152, 375-384.
21. Hoyer Fender, S., Costanzi, C., and Pehrson, J. R. (2000) Histone macroH2A1.2 is concentrated in the XY-body by the early pachytene stage of spermatogenesis, Exp. Cell Res. 258, 254-260.
22. Richler, C., Dhara, S. K., and Wahrman, J. (2000) Histone macroH2A1.2 is concentrated in the XY compartment of mammalian male meiotic nuclei, Cytogenet. Cell Genet. 89, 118-120.
23. Rasmussen, T. P., Huang, T., Mastrangelo, M. A., Loring, J., Panning, B., and Jaenisch, R. (1999) Messenger RNAs encoding mouse histone macroH2A1 isoforms are expressed at similar levels in male and female cells and result from alternative splicing, Nucleic Acids Res. 27, 3685-3689.
24. Perche, P. Y., Vourc'h, C., Konecny, L., Souchier, C., Robert-Nicoud, M., Dimitrov, S., and Khochbin, S. (2000) Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density, Curr. Biol. 10, 1531-1534.
25. Turner, J. M., Burgoyne, P. S., and Singh, P. B. (2001) M31 and macroH2A1.2 colocalise at the pseudoautosomal region during mouse meiosis, J. Cell Sci. 114, 3367-3375.
26. Ausió, J., Dong, F., and van Holde, K. E. (1989) Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome, J. Mol. Biol. 206, 451-463.
27. Wang, X., and Ausió, J. (2001) Histones are the major chromosomal protein components of the sperm of the nemerteans Cerebratulus californiensis and Cerebratulus lacteus, J. Exp. Zoo. 290, 431-436.
28. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning, A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
29. Ausió, J., and van Holde, K. E. (1986) Histone hyperacetylation: its effects on nucleosome conformation and stability, Biochemistry 25, 1421-1428.
30. Wang, X., Moore, S. C., Laszckzak, M., and Ausió, J. (2000) Acetylation increases the α-helical content of the histone tails of the nucleosome, J. Biol. Chem. 275, 35013-35020.
31. Geourjon, C., and Deleage, G. (1994) SOPM: a self-optimized method for protein secondary structure prediction, Protein Eng. 7, 157-164.
32. Abbott, D. W., Ivanova, V. S., Wang, X., Bonner, W. M., and Ausió, J. (2001) Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation, J. Biol. Chem. 276, 41945-41949.
33. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
34. Ausió, J., and Moore, S. C. (1998) Reconstitution of chromatin complexes from high-performance liquid chromatography-purified histones, Methods 15, 333-342.
35. Yager, T. D., and van Holde, K. E. (1984) Dynamics and equilibria of nucleosomes at elevated ionic strength, J. Biol. Chem. 259, 4212-4222.
36. Hayes, J. J., and Lee, K. M. (1997) In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins. Methods 12, 2-9.
37. Garcia Ramirez, M., Dong, F., and Ausió, J. (1992) Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1, J. Biol. Chem. 267, 19587-19595.
38. van Holde, K. E., and Weischet, W. O. (1978) Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes, Biopolymers 17, 1387-1403.
39. Eickbush, T. H., and Moudrianakis, E. N. (1978) The histone core complex: an octamer assembled by two sets of protein-protein interactions, Biochemistry 17, 4955-4964.
40. Eisenberg, H. (1976) Biological Macromolecules and Polyelectrolytes in Solution, Clarendon Press, Oxford.
41. Ausió, J. (2000) Analytical ultracentrifugation and the characterization of chromatin structure, Biophys. Chem. 86, 141-153.
42. Simon, R. H., and Felsenfeld, G. (1979) A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite, Nucleic Acids Res. 6, 689-696.
43. Pehrson, J. R., and Fuji, R. N. (1998) Evolutionary conservation of histone macroH2A subtypes and domains, Nucleic Acids Res. 26, 2837-2842.
44. Costanzi, C., and Pehrson, J. R. (2001) MACROH2A2, a new member of the MARCOH2A core histone family, J. Biol Chem. 276, 21776-21784.
45. Itoh, T., Ausió, J., and Katagiri, C. (1997) Histone H1 variants as sperm-specific nuclear proteins of Rana catesbeiana and their role in maintaining a unique condensed state of sperm chromatin, Mol. Reprod. Dev. 47, 181-190.
46. Kasinsky, H. E. (1989) Specificity and distribution of sperm basic proteins, CRC Press Inc., Boca Raton, FL.
47. Saperas, N., Ausió, J., Lloris, D., and Chiva, M. (1994) On the evolution of protamines in bony fish: alternatives to the "retroviral horizontal transmission" hypothesis, J. Mol. Evol. 39, 282-295.
48. Hunt, J. G., Kasinsky, H. E., Elsey, R. M., Wright, C. L., Rice, P., Bell, J. E., Sharp, D. J., Kiss, A. J., Hunt, D. F., Arnott, D. P. et al. (1996) Protamines of reptiles, J. Biol. Chem. 271, 23547-23557.
49. Lewis, J. D., Abbott, D. W., and Ausio, J. (2003) A haploid affair: core histone transitions during spermatogenesis, Biochem. Cell Biol. 81, 8077-8091.
50. D' Anna, J. A., and Isenberg, I. (1974) Interactions of histone LAK (f2a2) with histones KAS (f2b) and GRK (f2a1), Biochemistry 13, 2098-2104.
51. Arents, G., Burlingame, R. W., Wang, B. C., Love, W. E., and Moudrianakis, E. N. (1991) The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix, Proc. Natl. Acad. Sci. U.S.A. 88, 10148-10152.
52. Karantza, V., Freire, E., and Moudrianakis, E. N. (2001) Thermodynamic studies of the core histones: stability of the octamer subunits is not altered by removal of their terminal domains, Biochemistry 40, 13114-13123.
53. Bauer, W. R., Hayes, J. J., White, J. H., and Wolffe, A. P. (1994) Nucleosome structural changes due to acetylation, J. Mol. Biol. 236, 685-690.
54. Ausió, J., Seger, D., and Eisenberg, H. (1984) Nucleosome core particle stability and conformational change. Effect of temperature, particle, and NaCl concentrations and cross-linking of histone H3 sulfhydryl groups, J. Mol. Biol. 176, 77-104.
55. Li, W., Nagaraja, S., Delcuve, G. P., Hendzel, M. J., and Davie, J. R. (1993) Effects of histone acetylation, ubiquitination, and variants on nucleosome stability, Biochem. J. 296, 737-744.
56. Gilbert, S. L., Pehrson, J. R., and Sharp, P. A. (2000) XIST RNA associates with specific regions of the inactive X chromatin, J. Biol. Chem. 275, 36491-36494.
57. Mermoud, J. E., Popova, B., Peters, A. H., Jenuwein, T., and Brockdorff, N. (2002) Histone H3 lysine 9 methylation occurs rapidly at the onset of random X chromosome inactivation, Curr. Biol. 12, 247-251.
58. Pittoggi, C., Renzi, L., Zaccagnini, G., Cimini, D., Degrassi, F., Giordano, R., Magnano, A. R., Lorenzini, R., Lavia, P., and Spadafora, C. (1999) A fraction of mouse sperm chromatin is organized in nucleosomal hypersensitive domains enriched in retroposon DNA, J. Cell Sci. 112, 3537-3548.
59. Gatewood, J. M., Cook, G. R., Balhorn, R., Schmid, C. W., and Bradbury, E. M. (1990) Isolation of four core histones from human sperm chromatin representing a minor subset of somatic histones, J. Biol. Chem. 265, 20662-20666.
60. Allen, M. D., Buckle, A. M., Cordell, S. C., Lowe, J., and Bycroft, M. (2003) The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the nonhistone domain of macroH2A, J. Mol. Biol. 330, 503-511.
61. Csankovszki, G., Panning, B., Bates, B., Pehrson, J. R., and Jaenisch, R. (1999) Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation, Nat. Genet. 22, 323-324.
62. Creighton, T. E. (1996) Proteins, 2nd ed., W. H. Freeman and Co., New York.